Jaime Vaquer‐Alicea

This study identifies an N-terminal ATTR fibril segment that promotes TTR amyloid nucleation and polymorphism through structural compatibility and templating activity.

This study shows TAF15 forms amyloid fibrils and propagates prion-like between cells, identifying specific motifs that drive its aggregation in vitro and in cells.

This study identifies CTE-like tau seeds in ALS/PDC brain and spinal cord using alanine mutational scanning, suggesting ALS/PDC is a CTE-like tauopathy.

This study identifies cysteine residues as critical for tau aggregation and propagation in cells, both spontaneously and when seeded.

This study shows DnaJB1 inhibits tau aggregation by binding its N-terminus in vitro and in cellular models, with interactions enhanced by polyanionic factors.

This study shows that β-amyloid induces microglial GPC4 and APOE, which increases neuronal tau pathology and toxicity.

This study shows that TDP-43 aggregation through prion-like seeding impairs its autoregulation, leading to dysfunction and loss of function in cells.

The paper identifies amino acids critical for tau strain propagation by analyzing their role in amyloid templating across different tauopathies.

This paper identifies two VHH antibodies that selectively bind pathogenic tau seeds in AD and related tauopathies, showing potential for therapeutic and diagnostic applications.

This study identifies that tau assemblies in a subset of essential tremor cases with tau pathology are conformationally similar to Alzheimer's disease and primary age-related tauopathy.

This study determines the structure of ATTRv-V30M amyloid fibrils from cardiac and nerve tissues using cryo-EM, finding structural homogeneity across tissues when transthyretin originates from the liver.

The paper determines the cryo-EM structure of Alzheimer's disease tau filaments bound by the PET ligand MK-6240, revealing key binding interactions that inform ligand design.

The paper uses an in silico alanine scan method to identify energetically important interactions in tau amyloid fibrils and classifies structures using machine learning.

The paper identifies specific glycosaminoglycan (GAG) structural requirements for the uptake of Tau, Aβ, and α-synuclein aggregates by cells.